Inactivation of glutamine synthetases by an NAD:arginine ADP-ribosyltransferase.

This publication has 24 references indexed in Scilit:

• Effects of nucleotides on activity of a purified ADP-ribosyltransferase from turkey erythrocytes
  Archives of Biochemistry and Biophysics, 1982
• Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein.
  Proceedings of the National Academy of Sciences, 1982
• Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase
  Proceedings of the National Academy of Sciences, 1978
• Activation of Adenylate Cyclase by Heat-Labile Escherichia Coli Enterotoxin
  Journal of Clinical Investigation, 1978
• ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.
  Proceedings of the National Academy of Sciences, 1978
• Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system
  Proceedings of the National Academy of Sciences, 1978
• Diphtheria Toxin
  Annual Review of Biochemistry, 1977
• Poly (ADP-Ribose) and ADP-Ribosylation of Proteins
  Annual Review of Biochemistry, 1977
• Functional arginyl residues as ATP binding sites of glutamine synthetase and carbamyl phosphate synthetase.
  Proceedings of the National Academy of Sciences, 1975
• Regulation of Rat Liver Glutamine Synthetase: Activation by α-Ketoglutarate and Inhibition by Glycine, Alanine, and Carbamyl Phosphate
  Proceedings of the National Academy of Sciences, 1971